Document Detail


Colocalization of cystatin M/E and its target proteases suggests a role in terminal differentiation of human hair follicle and nail.
MedLine Citation:
PMID:  19005484     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The cysteine protease inhibitor cystatin M/E is a key regulator of a biochemical pathway that leads to epidermal terminal differentiation by inhibition of its target proteases cathepsin L, cathepsin V, and legumain. Inhibition of cathepsin L is important in the cornification process of the skin, as we have recently demonstrated that cathepsin L is the elusive processing and activating protease for transglutaminase 3, an enzyme that is responsible for crosslinking of structural proteins in cornified envelope formation. Here, we study the localization of all players of this pathway in the human hair follicle and nail unit in order to elucidate their possible role in the biology of these epidermal appendages. We found that cathepsin L and transglutaminase 3 specifically colocalize in the hair bulb and the nail matrix, the regions that provide cells that terminally differentiate to the hair fiber and the nail plate, respectively. Furthermore, transglutaminase 3 also colocalizes with the structural proteins loricrin and involucrin, which are established transglutaminase substrates. These findings suggest that cathepsin L and transglutaminase 3 could be involved in the pathway that leads to terminal differentiation, not only in the epidermis but also in the human hair follicle and nail unit.
Authors:
Tsing Cheng; Ivonne M J J van Vlijmen-Willems; Kiyotaka Hitomi; Marcel C Pasch; Piet E J van Erp; Joost Schalkwijk; Patrick L J M Zeeuwen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-11-13
Journal Detail:
Title:  The Journal of investigative dermatology     Volume:  129     ISSN:  1523-1747     ISO Abbreviation:  J. Invest. Dermatol.     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-04-16     Completed Date:  2009-05-01     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0426720     Medline TA:  J Invest Dermatol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1232-42     Citation Subset:  IM    
Affiliation:
Department of Dermatology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands.
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MeSH Terms
Descriptor/Qualifier:
Cathepsin L
Cathepsins / metabolism*
Cell Differentiation / physiology*
Cystatin M / metabolism*
Cysteine Endopeptidases / metabolism*
Hair Follicle / cytology,  metabolism*
Humans
Membrane Proteins / metabolism
Nails / cytology,  metabolism*
Protein Precursors / metabolism
Signal Transduction / physiology
Transglutaminases / metabolism*
Chemical
Reg. No./Substance:
0/CST6 protein, human; 0/Cystatin M; 0/Membrane Proteins; 0/Protein Precursors; 0/loricrin; 60108-77-2/involucrin; EC 2.3.2.13/TGM3 protein, human; EC 2.3.2.13/Transglutaminases; EC 3.4.-/Cathepsins; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.15/CTSL1 protein, human; EC 3.4.22.15/Cathepsin L

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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